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Updated: May 11, 2026

OLIgo Mass Profiling (OLIMP) of Extracellular Polysaccharides
Published on: June 20, 2010
Crystallization and preliminary X-ray diffraction analysis of a new xyloglucanase from Xanthomonas campestris pv.
Evandro Ares de Araújo1, Atílio Tomazini, Marco Antonio Seiki Kadowaki
1Instituto de Física de São Carlos, Universidade de São Paulo, 400 Trabalhador Saocarlense, 13566-590 São Carlos, SP, Brazil.
Abstract:
Xyloglucanases (Xghs) are important enzymes involved in xyloglucan modification and degradation. Xanthomonas campestris pv. campestris (Xcc) is a phytopathogenic bacterium which produces a large number of glycosyl hydrolases (GH), but has only one family 74 GH (Xcc-Xgh). This enzyme was overexpressed in Escherichia coli, purified and crystallized. Diffraction data sets were collected for the native enzyme and its complex with glucose to maximum resolutions of 2.0 and 2.1 Å, respectively. The data were indexed in a hexagonal crystal system with unit-cell parameters a = b = 153.4, c = 84.9 Å. As indicated by molecular-replacement solution, the crystals belonged to space group P6(1).
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